RBM10_HUMAN
ID RBM10_HUMAN Reviewed; 930 AA.
AC P98175; A0A0A0MR66; C4AM81; Q14136; Q5JRR2; Q9BTE4; Q9BTX0; Q9NTB1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 3.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=RNA-binding protein 10 {ECO:0000305};
DE AltName: Full=G patch domain-containing protein 9;
DE AltName: Full=RNA-binding motif protein 10;
DE AltName: Full=RNA-binding protein S1-1 {ECO:0000250|UniProtKB:P70501};
DE Short=S1-1;
GN Name=RBM10 {ECO:0000312|HGNC:HGNC:9896};
GN Synonyms=DXS8237E, GPATC9, GPATCH9, KIAA0122;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV. The
RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Brain, Lung, Muscle, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 544-930.
RC TISSUE=Fetal brain;
RX PubMed=8808293; DOI=10.1006/geno.1996.0022;
RA Coleman M.P., Ambrose H.J., Carrel L., Nemeth A.H., Willard H.F.,
RA Davies K.E.;
RT "A novel gene, DXS8237E, lies within 20 kb upstream of UBE1 in Xp11.23 and
RT has a different X inactivation status.";
RL Genomics 31:135-138(1996).
RN [8]
RP ASSOCIATION WITH THE SPLICEOSOME, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12176931; DOI=10.1101/gr.473902;
RA Rappsilber J., Ryder U., Lamond A.I., Mann M.;
RT "Large-scale proteomic analysis of the human spliceosome.";
RL Genome Res. 12:1231-1245(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-797, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-723; SER-733; SER-736
RP AND SER-738, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 (ISOFORM 5),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733; SER-736; SER-738 AND
RP SER-797, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-383, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP INVOLVEMENT IN TARPS.
RX PubMed=20451169; DOI=10.1016/j.ajhg.2010.04.007;
RA Johnston J.J., Teer J.K., Cherukuri P.F., Hansen N.F., Loftus S.K.,
RA Chong K., Mullikin J.C., Biesecker L.G.;
RT "Massively parallel sequencing of exons on the X chromosome identifies
RT RBM10 as the gene that causes a syndromic form of cleft palate.";
RL Am. J. Hum. Genet. 86:743-748(2010).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 5), PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-89; SER-718; SER-723; SER-738; SER-781 AND
RP SER-797, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 (ISOFORM 5),
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 5), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 5), PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-718; SER-723; SER-736 AND SER-797,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 (ISOFORM 5), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 5), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; SER-723; SER-736; SER-797
RP AND SER-845, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; SER-718; SER-723; SER-736
RP AND SER-738, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-902, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [23]
RP IDENTIFICATION IN A LARGE CHROMATIN REMODELING COMPLEX.
RX PubMed=17707232; DOI=10.1016/j.molcel.2007.07.024;
RA Zhu P., Zhou W., Wang J., Puc J., Ohgi K.A., Erdjument-Bromage H.,
RA Tempst P., Glass C.K., Rosenfeld M.G.;
RT "A histone H2A deubiquitinase complex coordinating histone acetylation and
RT H1 dissociation in transcriptional regulation.";
RL Mol. Cell 27:609-621(2007).
RN [24]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18315527; DOI=10.1042/bc20070142;
RA Inoue A., Tsugawa K., Tokunaga K., Takahashi K.P., Uni S., Kimura M.,
RA Nishio K., Yamamoto N., Honda K., Watanabe T., Yamane H., Tani T.;
RT "S1-1 nuclear domains: characterization and dynamics as a function of
RT transcriptional activity.";
RL Biol. Cell 100:523-535(2008).
RN [25]
RP FUNCTION, AND MIRNA-BINDING.
RX PubMed=28431233; DOI=10.1016/j.molcel.2017.03.014;
RA Treiber T., Treiber N., Plessmann U., Harlander S., Daiss J.L., Eichner N.,
RA Lehmann G., Schall K., Urlaub H., Meister G.;
RT "A Compendium of RNA-Binding Proteins that Regulate MicroRNA Biogenesis.";
RL Mol. Cell 66:270-284(2017).
RN [26]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-396.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May be involved in post-transcriptional processing, most
CC probably in mRNA splicing. Binds to RNA homopolymers, with a preference
CC for poly(G) and poly(U) and little for poly(A) (By similarity). May
CC bind to specific miRNA hairpins (PubMed:28431233).
CC {ECO:0000250|UniProtKB:P70501, ECO:0000269|PubMed:18315527,
CC ECO:0000269|PubMed:28431233}.
CC -!- SUBUNIT: Associates with the spliceosome. Component of a large
CC chromatin remodeling complex, at least composed of MYSM1, PCAF, RBM10
CC and KIF11/TRIP5. {ECO:0000269|PubMed:17707232}.
CC -!- INTERACTION:
CC P98175; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-721525, EBI-742750;
CC P98175; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-721525, EBI-10181188;
CC P98175; Q75N03: CBLL1; NbExp=3; IntAct=EBI-721525, EBI-2832762;
CC P98175; Q8NHQ1: CEP70; NbExp=6; IntAct=EBI-721525, EBI-739624;
CC P98175; Q8N684-3: CPSF7; NbExp=6; IntAct=EBI-721525, EBI-11523759;
CC P98175; Q92841: DDX17; NbExp=6; IntAct=EBI-721525, EBI-746012;
CC P98175; O43143: DHX15; NbExp=3; IntAct=EBI-721525, EBI-1237044;
CC P98175; Q92620: DHX38; NbExp=2; IntAct=EBI-721525, EBI-1043041;
CC P98175; Q92917: GPKOW; NbExp=2; IntAct=EBI-721525, EBI-746309;
CC P98175; Q13123: IK; NbExp=2; IntAct=EBI-721525, EBI-713456;
CC P98175; Q5VWX1: KHDRBS2; NbExp=3; IntAct=EBI-721525, EBI-742808;
CC P98175; Q13351: KLF1; NbExp=3; IntAct=EBI-721525, EBI-8284732;
CC P98175; Q96DN6: MBD6; NbExp=3; IntAct=EBI-721525, EBI-719591;
CC P98175; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-721525, EBI-16439278;
CC P98175; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-721525, EBI-11022007;
CC P98175; Q9GZV8: PRDM14; NbExp=6; IntAct=EBI-721525, EBI-3957793;
CC P98175; Q9UMS4: PRPF19; NbExp=2; IntAct=EBI-721525, EBI-395746;
CC P98175; P86478: PRR20E; NbExp=3; IntAct=EBI-721525, EBI-12700196;
CC P98175; P26599: PTBP1; NbExp=4; IntAct=EBI-721525, EBI-350540;
CC P98175; P26599-3: PTBP1; NbExp=3; IntAct=EBI-721525, EBI-16437588;
CC P98175; Q9UKA9-2: PTBP2; NbExp=3; IntAct=EBI-721525, EBI-12255608;
CC P98175; P98175: RBM10; NbExp=2; IntAct=EBI-721525, EBI-721525;
CC P98175; Q15415: RBMY1J; NbExp=3; IntAct=EBI-721525, EBI-8642021;
CC P98175; Q15459: SF3A1; NbExp=2; IntAct=EBI-721525, EBI-1054743;
CC P98175; Q15427: SF3B4; NbExp=8; IntAct=EBI-721525, EBI-348469;
CC P98175; P09234: SNRPC; NbExp=2; IntAct=EBI-721525, EBI-766589;
CC P98175; Q8IWZ8: SUGP1; NbExp=2; IntAct=EBI-721525, EBI-2691671;
CC P98175; Q13148: TARDBP; NbExp=3; IntAct=EBI-721525, EBI-372899;
CC P98175; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-721525, EBI-8787464;
CC P98175; Q9NVV9: THAP1; NbExp=6; IntAct=EBI-721525, EBI-741515;
CC P98175; Q08117: TLE5; NbExp=3; IntAct=EBI-721525, EBI-717810;
CC P98175; P26368: U2AF2; NbExp=2; IntAct=EBI-721525, EBI-742339;
CC P98175; O15042: U2SURP; NbExp=2; IntAct=EBI-721525, EBI-310697;
CC P98175; O43167: ZBTB24; NbExp=3; IntAct=EBI-721525, EBI-744471;
CC P98175; Q9NTW7: ZFP64; NbExp=3; IntAct=EBI-721525, EBI-711679;
CC P98175; Q9NSD4: ZNF275; NbExp=3; IntAct=EBI-721525, EBI-17263125;
CC P98175; Q96PQ6: ZNF317; NbExp=3; IntAct=EBI-721525, EBI-1210473;
CC P98175; Q9H9D4: ZNF408; NbExp=3; IntAct=EBI-721525, EBI-347633;
CC P98175; Q8WTR7: ZNF473; NbExp=3; IntAct=EBI-721525, EBI-751409;
CC P98175; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-721525, EBI-11035148;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18315527}. Note=In
CC the extranucleolar nucleoplasm constitutes hundreds of nuclear domains,
CC which dynamically change their structures in a reversible manner. Upon
CC globally reducing RNA polymerase II transcription, the nuclear bodies
CC enlarge and decrease in number. They occur closely adjacent to nuclear
CC speckles or IGCs (interchromatin granule clusters) but coincide with
CC TIDRs (transcription-inactivation-dependent RNA domains).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=6;
CC Name=1;
CC IsoId=P98175-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P98175-2; Sequence=VSP_036035;
CC Name=3;
CC IsoId=P98175-3; Sequence=VSP_036173;
CC Name=4;
CC IsoId=P98175-4; Sequence=VSP_036173, VSP_036035;
CC Name=5;
CC IsoId=P98175-5; Sequence=VSP_059341;
CC Name=Ribosome biogenesis inhibitor MINAS-60;
CC IsoId=P0DW28-1; Sequence=External;
CC -!- DISEASE: TARP syndrome (TARPS) [MIM:311900]: A disorder characterized
CC by the Robin sequence (micrognathia, glossoptosis and cleft palate),
CC talipes equinovarus and cardiac defects. {ECO:0000269|PubMed:20451169}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- MISCELLANEOUS: RBM10 transcripts also code for an alternative open
CC reading frame (alt-ORF) coding for the MINAS-60 (AC P0DW28) protein
CC (Probable). MINAS-60 and RBM10 ORFs are overlapping and are formed by
CC shifting the reading frame (Probable). {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB33572.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA09471.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB70731.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB70731.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D50912; BAA09471.1; ALT_INIT; mRNA.
DR EMBL; AK292758; BAF85447.1; -; mRNA.
DR EMBL; AL137421; CAB70731.1; ALT_SEQ; mRNA.
DR EMBL; AL513366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471164; EAW59284.1; -; Genomic_DNA.
DR EMBL; CH471164; EAW59285.1; -; Genomic_DNA.
DR EMBL; CH471164; EAW59286.1; -; Genomic_DNA.
DR EMBL; CH471164; EAW59287.1; -; Genomic_DNA.
DR EMBL; CH471164; EAW59283.1; -; Genomic_DNA.
DR EMBL; BC003089; AAH03089.1; -; mRNA.
DR EMBL; BC004181; AAH04181.1; -; mRNA.
DR EMBL; BC008733; AAH08733.1; -; mRNA.
DR EMBL; BC024153; AAH24153.1; -; mRNA.
DR EMBL; U35373; AAB33572.1; ALT_FRAME; mRNA.
DR CCDS; CCDS14274.1; -. [P98175-1]
DR CCDS; CCDS56600.1; -. [P98175-3]
DR CCDS; CCDS75969.1; -. [P98175-5]
DR CCDS; CCDS78478.1; -. [P98175-4]
DR RefSeq; NP_001191395.1; NM_001204466.1. [P98175-3]
DR RefSeq; NP_001191396.1; NM_001204467.1. [P98175-2]
DR RefSeq; NP_001191397.1; NM_001204468.1. [P98175-5]
DR RefSeq; NP_005667.2; NM_005676.4. [P98175-1]
DR RefSeq; NP_690595.1; NM_152856.2. [P98175-4]
DR PDB; 2LXI; NMR; -; A=128-218.
DR PDB; 2M2B; NMR; -; A=277-408.
DR PDB; 2MXV; NMR; -; A=211-250.
DR PDB; 2MXW; NMR; -; A=558-646.
DR PDB; 5ZSW; NMR; -; A=300-385.
DR PDB; 5ZSY; NMR; -; A=300-385.
DR PDBsum; 2LXI; -.
DR PDBsum; 2M2B; -.
DR PDBsum; 2MXV; -.
DR PDBsum; 2MXW; -.
DR PDBsum; 5ZSW; -.
DR PDBsum; 5ZSY; -.
DR AlphaFoldDB; P98175; -.
DR BMRB; P98175; -.
DR SMR; P98175; -.
DR BioGRID; 113869; 216.
DR IntAct; P98175; 108.
DR MINT; P98175; -.
DR STRING; 9606.ENSP00000328848; -.
DR MoonDB; P98175; Predicted.
DR GlyGen; P98175; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P98175; -.
DR MetOSite; P98175; -.
DR PhosphoSitePlus; P98175; -.
DR BioMuta; RBM10; -.
DR DMDM; 218512116; -.
DR EPD; P98175; -.
DR jPOST; P98175; -.
DR MassIVE; P98175; -.
DR MaxQB; P98175; -.
DR PaxDb; P98175; -.
DR PeptideAtlas; P98175; -.
DR PRIDE; P98175; -.
DR ProteomicsDB; 57810; -. [P98175-1]
DR ProteomicsDB; 57811; -. [P98175-2]
DR ProteomicsDB; 57812; -. [P98175-3]
DR ProteomicsDB; 57813; -. [P98175-4]
DR Antibodypedia; 11142; 208 antibodies from 29 providers.
DR DNASU; 8241; -.
DR Ensembl; ENST00000329236.8; ENSP00000328848.8; ENSG00000182872.16. [P98175-5]
DR Ensembl; ENST00000345781.10; ENSP00000329659.6; ENSG00000182872.16. [P98175-3]
DR Ensembl; ENST00000377604.8; ENSP00000366829.3; ENSG00000182872.16. [P98175-1]
DR Ensembl; ENST00000628161.2; ENSP00000486115.1; ENSG00000182872.16. [P98175-4]
DR GeneID; 8241; -.
DR KEGG; hsa:8241; -.
DR MANE-Select; ENST00000377604.8; ENSP00000366829.3; NM_005676.5; NP_005667.2.
DR UCSC; uc004dhf.4; human. [P98175-1]
DR UCSC; uc004dhi.4; human.
DR CTD; 8241; -.
DR DisGeNET; 8241; -.
DR GeneCards; RBM10; -.
DR HGNC; HGNC:9896; RBM10.
DR HPA; ENSG00000182872; Low tissue specificity.
DR MalaCards; RBM10; -.
DR MIM; 300080; gene.
DR MIM; 311900; phenotype.
DR neXtProt; NX_P98175; -.
DR OpenTargets; ENSG00000182872; -.
DR Orphanet; 2886; TARP syndrome.
DR PharmGKB; PA34259; -.
DR VEuPathDB; HostDB:ENSG00000182872; -.
DR eggNOG; KOG0154; Eukaryota.
DR GeneTree; ENSGT00940000160369; -.
DR InParanoid; P98175; -.
DR OMA; QYYTEYY; -.
DR OrthoDB; 786674at2759; -.
DR PhylomeDB; P98175; -.
DR TreeFam; TF315789; -.
DR PathwayCommons; P98175; -.
DR SignaLink; P98175; -.
DR SIGNOR; P98175; -.
DR BioGRID-ORCS; 8241; 127 hits in 723 CRISPR screens.
DR ChiTaRS; RBM10; human.
DR GeneWiki; RBM10; -.
DR GenomeRNAi; 8241; -.
DR Pharos; P98175; Tbio.
DR PRO; PR:P98175; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P98175; protein.
DR Bgee; ENSG00000182872; Expressed in right hemisphere of cerebellum and 193 other tissues.
DR ExpressionAtlas; P98175; baseline and differential.
DR Genevisible; P98175; HS.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:1905461; P:positive regulation of vascular associated smooth muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IEA:InterPro.
DR GO; GO:1905288; P:vascular associated smooth muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:1990874; P:vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR CDD; cd16167; OCRE_RBM10; 1.
DR CDD; cd12754; RRM2_RBM10; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR041591; OCRE.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR033095; RBM10.
DR InterPro; IPR035618; RBM10_OCRE.
DR InterPro; IPR034992; RBM10_RRM2.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR13948:SF4; PTHR13948:SF4; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF17780; OCRE; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; Alternative splicing;
KW Metal-binding; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..930
FT /note="RNA-binding protein 10"
FT /id="PRO_0000081767"
FT DOMAIN 129..209
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 300..384
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 858..904
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT ZN_FING 212..242
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 759..784
FT /note="C2H2-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..126
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 383
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 797
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 902
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 1
FT /note="M -> MSGSPSLTARAEKVSVDAGRGGGESLQEASPRLADHGSSSGGGWEVK
FT RSQRLRRGPSSPRRPYQDM (in isoform 5)"
FT /id="VSP_059341"
FT VAR_SEQ 68..144
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_036173"
FT VAR_SEQ 354
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8590280"
FT /id="VSP_036035"
FT VARIANT 396
FT /note="R -> H (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035486"
FT CONFLICT 499
FT /note="A -> P (in Ref. 1; BAA09471)"
FT /evidence="ECO:0000305"
FT CONFLICT 672
FT /note="S -> T (in Ref. 3; CAB70731)"
FT /evidence="ECO:0000305"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:2LXI"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:2LXI"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2LXI"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2LXI"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:2LXI"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:2LXI"
FT TURN 190..193
FT /evidence="ECO:0007829|PDB:2LXI"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:2LXI"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:2LXI"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2MXV"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2MXV"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:2M2B"
FT HELIX 314..320
FT /evidence="ECO:0007829|PDB:2M2B"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:2M2B"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:2M2B"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:2M2B"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:2M2B"
FT HELIX 355..363
FT /evidence="ECO:0007829|PDB:2M2B"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:5ZSW"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:2M2B"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:5ZSW"
FT HELIX 569..571
FT /evidence="ECO:0007829|PDB:2MXW"
FT STRAND 572..574
FT /evidence="ECO:0007829|PDB:2MXW"
FT TURN 576..578
FT /evidence="ECO:0007829|PDB:2MXW"
FT TURN 584..586
FT /evidence="ECO:0007829|PDB:2MXW"
FT STRAND 597..599
FT /evidence="ECO:0007829|PDB:2MXW"
FT TURN 600..603
FT /evidence="ECO:0007829|PDB:2MXW"
FT STRAND 604..608
FT /evidence="ECO:0007829|PDB:2MXW"
FT TURN 610..612
FT /evidence="ECO:0007829|PDB:2MXW"
FT STRAND 614..617
FT /evidence="ECO:0007829|PDB:2MXW"
FT STRAND 622..624
FT /evidence="ECO:0007829|PDB:2MXW"
FT STRAND 627..630
FT /evidence="ECO:0007829|PDB:2MXW"
FT INIT_MET P98175-5:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES P98175-5:2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES P98175-5:30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
SQ SEQUENCE 930 AA; 103533 MW; 472E68F085CA5744 CRC64;
MEYERRGGRG DRTGRYGATD RSQDDGGENR SRDHDYRDMD YRSYPREYGS QEGKHDYDDS
SEEQSAEDSY EASPGSETQR RRRRRHRHSP TGPPGFPRDG DYRDQDYRTE QGEEEEEEED
EEEEEKASNI VMLRMLPQAA TEDDIRGQLQ SHGVQAREVR LMRNKSSGQS RGFAFVEFSH
LQDATRWMEA NQHSLNILGQ KVSMHYSDPK PKINEDWLCN KCGVQNFKRR EKCFKCGVPK
SEAEQKLPLG TRLDQQTLPL GGRELSQGLL PLPQPYQAQG VLASQALSQG SEPSSENAND
TIILRNLNPH STMDSILGAL APYAVLSSSN VRVIKDKQTQ LNRGFAFIQL STIVEAAQLL
QILQALHPPL TIDGKTINVE FAKGSKRDMA SNEGSRISAA SVASTAIAAA QWAISQASQG
GEGTWATSEE PPVDYSYYQQ DEGYGNSQGT ESSLYAHGYL KGTKGPGITG TKGDPTGAGP
EASLEPGADS VSMQAFSRAQ PGAAPGIYQQ SAEASSSQGT AANSQSYTIM SPAVLKSELQ
SPTHPSSALP PATSPTAQES YSQYPVPDVS TYQYDETSGY YYDPQTGLYY DPNSQYYYNA
QSQQYLYWDG ERRTYVPALE QSADGHKETG APSKEGKEKK EKHKTKTAQQ IAKDMERWAR
SLNKQKENFK NSFQPISSLR DDERRESATA DAGYAILEKK GALAERQHTS MDLPKLASDD
RPSPPRGLVA AYSGESDSEE EQERGGPERE EKLTDWQKLA CLLCRRQFPS KEALIRHQQL
SGLHKQNLEI HRRAHLSENE LEALEKNDME QMKYRDRAAE RREKYGIPEP PEPKRRKYGG
ISTASVDFEQ PTRDGLGSDN IGSRMLQAMG WKEGSGLGRK KQGIVTPIEA QTRVRGSGLG
ARGSSYGVTS TESYKETLHK TMVTRFNEAQ
